Advanced

Enrichment of phosphoproteins and phosphopeptide derivatization identify universal stress proteins in elicitor-treated Arabidopsis

Lenman, Marit LU ; Sörensson, Carolin LU and Andreasson, Erik LU (2008) In Molecular Plant-Microbe Interactions 21(10). p.1275-1284
Abstract
Protein phosphorylation is a key biological process that regulates reactions involved in plant-microbe interactions. The phosphorylated form of a protein often represents only a small fraction of the total population and can be problematic to analyze in a mass spectrometer. We demonstrate how a titanium dioxide (TiO2) resin can be employed for the enrichment of phosphoproteins, as well as a method to derivatize TiO2-purified phosphopeptides to facilitate determination of the exact site of phosphorylation. The use of these methods was exemplified by the identification of two plant proteins that were shown to be phosphorylated after the elicitation of Arabidopsis cells with Phytophthora infestans zoospores and xylanase. Both of the proteins... (More)
Protein phosphorylation is a key biological process that regulates reactions involved in plant-microbe interactions. The phosphorylated form of a protein often represents only a small fraction of the total population and can be problematic to analyze in a mass spectrometer. We demonstrate how a titanium dioxide (TiO2) resin can be employed for the enrichment of phosphoproteins, as well as a method to derivatize TiO2-purified phosphopeptides to facilitate determination of the exact site of phosphorylation. The use of these methods was exemplified by the identification of two plant proteins that were shown to be phosphorylated after the elicitation of Arabidopsis cells with Phytophthora infestans zoospores and xylanase. Both of the proteins that were identified, At5g54430.1 and At4g27320.1, were found to contain a universal stress protein domain with conserved residues for ATP binding. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
4-sulfophenyl isothiocyanate, SPITC
in
Molecular Plant-Microbe Interactions
volume
21
issue
10
pages
1275 - 1284
publisher
American Physical Society
external identifiers
  • wos:000259330000001
  • scopus:54949125683
ISSN
0894-0282
DOI
10.1094/MPMI-21-10-1275
language
English
LU publication?
yes
id
c5f80f33-bc70-4dce-b116-dc9ee8318587 (old id 1246646)
date added to LUP
2008-11-18 13:21:13
date last changed
2017-01-22 03:23:53
@article{c5f80f33-bc70-4dce-b116-dc9ee8318587,
  abstract     = {Protein phosphorylation is a key biological process that regulates reactions involved in plant-microbe interactions. The phosphorylated form of a protein often represents only a small fraction of the total population and can be problematic to analyze in a mass spectrometer. We demonstrate how a titanium dioxide (TiO2) resin can be employed for the enrichment of phosphoproteins, as well as a method to derivatize TiO2-purified phosphopeptides to facilitate determination of the exact site of phosphorylation. The use of these methods was exemplified by the identification of two plant proteins that were shown to be phosphorylated after the elicitation of Arabidopsis cells with Phytophthora infestans zoospores and xylanase. Both of the proteins that were identified, At5g54430.1 and At4g27320.1, were found to contain a universal stress protein domain with conserved residues for ATP binding.},
  author       = {Lenman, Marit and Sörensson, Carolin and Andreasson, Erik},
  issn         = {0894-0282},
  keyword      = {4-sulfophenyl isothiocyanate,SPITC},
  language     = {eng},
  number       = {10},
  pages        = {1275--1284},
  publisher    = {American Physical Society},
  series       = {Molecular Plant-Microbe Interactions},
  title        = {Enrichment of phosphoproteins and phosphopeptide derivatization identify universal stress proteins in elicitor-treated Arabidopsis},
  url          = {http://dx.doi.org/10.1094/MPMI-21-10-1275},
  volume       = {21},
  year         = {2008},
}